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P08515 (GST26_SCHJA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase class-mu 26 kDa isozyme

Short name=GST 26
EC=2.5.1.18
Alternative name(s):
Sj26 antigen
SjGST
OrganismSchistosoma japonicum (Blood fluke)
Taxonomic identifier6182 [NCBI]
Taxonomic lineageEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma

Protein attributes

Sequence length218 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.

GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut.

Catalytic activity

RX + glutathione = HX + R-S-glutathione.

Subunit structure

Homodimer.

Miscellaneous

There are at least two isoenzymes of GST in S.japonicum.

Sequence similarities

Belongs to the GST superfamily. Mu family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Ontologies

Keywords
   Molecular functionTransferase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Molecular_functionglutathione transferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 218217Glutathione S-transferase class-mu 26 kDa isozyme
PRO_0000185805

Regions

Domain2 – 8382GST N-terminal
Domain85 – 203119GST C-terminal
Region7 – 82Glutathione binding
Region41 – 455Glutathione binding
Region54 – 552Glutathione binding
Region67 – 682Glutathione binding

Sites

Binding site1111Substrate Probable

Secondary structure

....................................... 218
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08515 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 5E2AC418BD0EF13F

FASTA21825,499
        10         20         30         40         50         60 
MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID 

        70         80         90        100        110        120 
GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV 

       130        140        150        160        170        180 
DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALD VVLYMDPMCL DAFPKLVCFK 

       190        200        210 
KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPK 

« Hide

References

[1]"Mr 26,000 antigen of Schistosoma japonicum recognized by resistant WEHI 129/J mice is a parasite glutathione S-transferase."
Smith D.B., Davern K.M., Board P.G., Tiu W.U., Garcia E.G., Mitchell G.F.
Proc. Natl. Acad. Sci. U.S.A. 83:8703-8707(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Smith D.B., Davern K.M., Board P.G., Tiu W.U., Garcia E.G., Mitchell G.F.
Proc. Natl. Acad. Sci. U.S.A. 84:6541-6541(1987)
Cited for: SEQUENCE REVISION.
[3]"Expression of an enzymatically active parasite molecule in Escherichia coli: Schistosoma japonicum glutathione S-transferase."
Smith D.B., Rubira M.R., Simpson R.J., Davern K.M., Tiu W.U., Board P.G., Mitchell G.F.
Mol. Biochem. Parasitol. 27:249-256(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-15.
[4]"Three-dimensional structure of Schistosoma japonicum glutathione S-transferase fused with a six-amino acid conserved neutralizing epitope of gp41 from HIV."
Lim K., Ho J.X., Keeling K., Gilliland G.L., Ji X., Ruker F., Carter D.C.
Protein Sci. 3:2233-2244(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[5]"Crystal structures of a schistosomal drug and vaccine target: glutathione S-transferase from Schistosoma japonica and its complex with the leading antischistosomal drug praziquantel."
McTigue M.A., Williams D.R., Tainer J.A.
J. Mol. Biol. 246:21-27(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH INHIBITOR PRAZIQUANTEL.
[6]"Characterization of the electrophile binding site and substrate binding mode of the 26-kDa glutathione S-transferase from Schistosoma japonicum."
Cardoso R.M., Daniels D.S., Bruns C.M., Tainer J.A.
Proteins 51:137-146(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE ANALOGS.
[7]"Using affinity chromatography to engineer and characterize pH-dependent protein switches."
Sagermann M., Chapleau R.R., DeLorimier E., Lei M.
Protein Sci. 18:217-228(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-214.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M14654 mRNA. Translation: AAB59203.1.
PIRA61514.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B8XX-ray2.70A2-218[»]
1BG5X-ray2.60A1-218[»]
1DUGX-ray1.80A/B2-218[»]
1GNEX-ray2.50A1-218[»]
1GTAX-ray2.40A1-218[»]
1GTBX-ray2.60A1-218[»]
1M99X-ray2.30A1-218[»]
1M9AX-ray2.10A1-218[»]
1M9BX-ray2.60A1-218[»]
1U87X-ray3.50A1-218[»]
1U88X-ray3.50A/B1-218[»]
1UA5X-ray2.50A1-218[»]
1Y6EX-ray3.00A/B2-217[»]
3CRTX-ray1.90A1-214[»]
3CRUX-ray2.30A1-214[»]
3D0ZX-ray2.50A1-214[»]
3QMZX-ray6.00S/T2-218[»]
4AI6X-ray3.40A/B2-218[»]
4AKGX-ray3.30A/B2-218[»]
4AKHX-ray3.60A/B2-218[»]
4AKIX-ray3.70A/B2-218[»]
4ECBX-ray2.20A/B1-218[»]
4ECCX-ray2.20A1-218[»]
ProteinModelPortalP08515.
SMRP08515. Positions 2-218.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING6182.P08515.

Chemistry

DrugBankDB00143. Glutathione.
DB01058. Praziquantel.

Proteomic databases

PRIDEP08515.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG300089.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP08515.

Entry information

Entry nameGST26_SCHJA
AccessionPrimary (citable) accession number: P08515
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 103 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references